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Mining electron density for functionally relevant protein polysterism in crystal structures
This review focuses on conceptual and methodological advances in our understanding and characterization of the conformational heterogeneity of proteins. Focusing on X-ray crystallography, we describe how polysterism, the interconversion of pre-existing conformational substates, has traditionally bee...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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SP Birkhäuser Verlag Basel
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3092063/ https://www.ncbi.nlm.nih.gov/pubmed/21190057 http://dx.doi.org/10.1007/s00018-010-0611-4 |
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author | Fraser, James S. Jackson, Colin J. |
author_facet | Fraser, James S. Jackson, Colin J. |
author_sort | Fraser, James S. |
collection | PubMed |
description | This review focuses on conceptual and methodological advances in our understanding and characterization of the conformational heterogeneity of proteins. Focusing on X-ray crystallography, we describe how polysterism, the interconversion of pre-existing conformational substates, has traditionally been analyzed by comparing independent crystal structures or multiple chains within a single crystal asymmetric unit. In contrast, recent studies have focused on mining electron density maps to reveal previously ‘hidden’ minor conformational substates. Functional tests of the importance of minor states suggest that evolutionary selection shapes the entire conformational landscape, including uniquely configured conformational substates, the relative distribution of these substates, and the speed at which the protein can interconvert between them. An increased focus on polysterism may shape the way protein structure and function is studied in the coming years. |
format | Text |
id | pubmed-3092063 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | SP Birkhäuser Verlag Basel |
record_format | MEDLINE/PubMed |
spelling | pubmed-30920632011-06-07 Mining electron density for functionally relevant protein polysterism in crystal structures Fraser, James S. Jackson, Colin J. Cell Mol Life Sci Review This review focuses on conceptual and methodological advances in our understanding and characterization of the conformational heterogeneity of proteins. Focusing on X-ray crystallography, we describe how polysterism, the interconversion of pre-existing conformational substates, has traditionally been analyzed by comparing independent crystal structures or multiple chains within a single crystal asymmetric unit. In contrast, recent studies have focused on mining electron density maps to reveal previously ‘hidden’ minor conformational substates. Functional tests of the importance of minor states suggest that evolutionary selection shapes the entire conformational landscape, including uniquely configured conformational substates, the relative distribution of these substates, and the speed at which the protein can interconvert between them. An increased focus on polysterism may shape the way protein structure and function is studied in the coming years. SP Birkhäuser Verlag Basel 2010-12-29 2011 /pmc/articles/PMC3092063/ /pubmed/21190057 http://dx.doi.org/10.1007/s00018-010-0611-4 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Review Fraser, James S. Jackson, Colin J. Mining electron density for functionally relevant protein polysterism in crystal structures |
title | Mining electron density for functionally relevant protein polysterism in crystal structures |
title_full | Mining electron density for functionally relevant protein polysterism in crystal structures |
title_fullStr | Mining electron density for functionally relevant protein polysterism in crystal structures |
title_full_unstemmed | Mining electron density for functionally relevant protein polysterism in crystal structures |
title_short | Mining electron density for functionally relevant protein polysterism in crystal structures |
title_sort | mining electron density for functionally relevant protein polysterism in crystal structures |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3092063/ https://www.ncbi.nlm.nih.gov/pubmed/21190057 http://dx.doi.org/10.1007/s00018-010-0611-4 |
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